Structural analysis of Borrelia burgdorferi periplasmic lipoprotein BB0365 involved in Lyme disease infection

Kalvis Brangulis; Inara Akopjana; Ivars Petrovskis; Andris Kazaks; Atis Jēkabsons; Kristaps Jaudzems; Artūrs Vīksna; Māris Bērtiņš; Kaspars Tars

doi:10.1002/1873-3468.13594

Structural analysis of Borrelia burgdorferi periplasmic lipoprotein BB0365 involved in Lyme disease infection

Kalvis Brangulis (Corresponding Author), Inara Akopjana, Ivars Petrovskis, Andris Kazaks, Atis Jēkabsons, Kristaps Jaudzems, Artūrs Vīksna, Māris Bērtiņš, Kaspars Tars

Research output: Contribution to journal › Article › peer-review

5 Citations (Scopus)

Abstract

The periplasmic lipoprotein BB0365 of the Lyme disease agent Borrelia burgdorferi is expressed throughout mammalian infection and is essential for all phases of Lyme disease infection; its function, however, remains unknown. In the current study, our structural analysis of BB0365 revealed the same structural fold as that found in the NqrC and RnfG subunits of the NADH:quinone and ferredoxin:NAD⁺ sodium-translocating oxidoreductase complexes, which points to a potential role for BB0365 as a component of the sodium pump. Additionally, BB0365 coordinated Zn²⁺ by the His51, His55, His140 residues, and the Zn²⁺-binding site indicates that BB0365 could act as a potential metalloenzyme; therefore, this structure narrows down the potential functions of BB0365, an essential protein for B. burgdorferi to cause Lyme disease.

Original language	English
Pages (from-to)	317-326
Number of pages	10
Journal	FEBS Letters
Volume	594
Issue number	2
DOIs	https://doi.org/10.1002/1873-3468.13594
Publication status	Published - 1 Jan 2020
Externally published	Yes

Keywords*

Ixodes ticks
Lyme borreliosis
Lyme disease
metalloenzyme
spirochete

Field of Science*

3.1 Basic medicine
1.6 Biological sciences

Publication Type*

1.1. Scientific article indexed in Web of Science and/or Scopus database

Access to Document

10.1002/1873-3468.13594

Cite this

@article{5f5717543ec64ac29134cbea860ce4b4,

title = "Structural analysis of Borrelia burgdorferi periplasmic lipoprotein BB0365 involved in Lyme disease infection",

abstract = "The periplasmic lipoprotein BB0365 of the Lyme disease agent Borrelia burgdorferi is expressed throughout mammalian infection and is essential for all phases of Lyme disease infection; its function, however, remains unknown. In the current study, our structural analysis of BB0365 revealed the same structural fold as that found in the NqrC and RnfG subunits of the NADH:quinone and ferredoxin:NAD+ sodium-translocating oxidoreductase complexes, which points to a potential role for BB0365 as a component of the sodium pump. Additionally, BB0365 coordinated Zn2+ by the His51, His55, His140 residues, and the Zn2+-binding site indicates that BB0365 could act as a potential metalloenzyme; therefore, this structure narrows down the potential functions of BB0365, an essential protein for B. burgdorferi to cause Lyme disease.",

keywords = "Ixodes ticks, Lyme borreliosis, Lyme disease, metalloenzyme, spirochete",

author = "Kalvis Brangulis and Inara Akopjana and Ivars Petrovskis and Andris Kazaks and Atis Jēkabsons and Kristaps Jaudzems and Artūrs Vīksna and Māris Bērtiņ{\v s} and Kaspars Tars",

note = "Funding Information: This work was supported by the European Regional Development Fund (ERDF) post-doctoral grant to KB, Nr. 1.1.1.2/VIAA/1/16/144 ?Structural and functional studies of Lyme disease agent Borrelia burgdorferi outer surface proteins to reveal the mechanisms of pathogenesis with the intention to create a new vaccine?. Diffraction data have been collected on BL14.1 at the BESSY II electron storage ring operated by the Helmholtz-Zentrum, Berlin. We would particularly like to acknowledge the help and support of Manfred S. Weiss and Christian Feiler during the experiment. Publisher Copyright: {\textcopyright} 2019 Federation of European Biochemical Societies Copyright: Copyright 2020 Elsevier B.V., All rights reserved.",

year = "2020",

month = jan,

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doi = "10.1002/1873-3468.13594",

language = "English",

volume = "594",

pages = "317--326",

journal = "FEBS Letters",

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T1 - Structural analysis of Borrelia burgdorferi periplasmic lipoprotein BB0365 involved in Lyme disease infection

AU - Brangulis, Kalvis

AU - Akopjana, Inara

AU - Petrovskis, Ivars

AU - Kazaks, Andris

AU - Jēkabsons, Atis

AU - Jaudzems, Kristaps

AU - Vīksna, Artūrs

AU - Bērtiņš, Māris

AU - Tars, Kaspars

N1 - Funding Information: This work was supported by the European Regional Development Fund (ERDF) post-doctoral grant to KB, Nr. 1.1.1.2/VIAA/1/16/144 ?Structural and functional studies of Lyme disease agent Borrelia burgdorferi outer surface proteins to reveal the mechanisms of pathogenesis with the intention to create a new vaccine?. Diffraction data have been collected on BL14.1 at the BESSY II electron storage ring operated by the Helmholtz-Zentrum, Berlin. We would particularly like to acknowledge the help and support of Manfred S. Weiss and Christian Feiler during the experiment. Publisher Copyright: © 2019 Federation of European Biochemical Societies Copyright: Copyright 2020 Elsevier B.V., All rights reserved.

PY - 2020/1/1

Y1 - 2020/1/1

N2 - The periplasmic lipoprotein BB0365 of the Lyme disease agent Borrelia burgdorferi is expressed throughout mammalian infection and is essential for all phases of Lyme disease infection; its function, however, remains unknown. In the current study, our structural analysis of BB0365 revealed the same structural fold as that found in the NqrC and RnfG subunits of the NADH:quinone and ferredoxin:NAD+ sodium-translocating oxidoreductase complexes, which points to a potential role for BB0365 as a component of the sodium pump. Additionally, BB0365 coordinated Zn2+ by the His51, His55, His140 residues, and the Zn2+-binding site indicates that BB0365 could act as a potential metalloenzyme; therefore, this structure narrows down the potential functions of BB0365, an essential protein for B. burgdorferi to cause Lyme disease.

AB - The periplasmic lipoprotein BB0365 of the Lyme disease agent Borrelia burgdorferi is expressed throughout mammalian infection and is essential for all phases of Lyme disease infection; its function, however, remains unknown. In the current study, our structural analysis of BB0365 revealed the same structural fold as that found in the NqrC and RnfG subunits of the NADH:quinone and ferredoxin:NAD+ sodium-translocating oxidoreductase complexes, which points to a potential role for BB0365 as a component of the sodium pump. Additionally, BB0365 coordinated Zn2+ by the His51, His55, His140 residues, and the Zn2+-binding site indicates that BB0365 could act as a potential metalloenzyme; therefore, this structure narrows down the potential functions of BB0365, an essential protein for B. burgdorferi to cause Lyme disease.

KW - Ixodes ticks

KW - Lyme borreliosis

KW - Lyme disease

KW - metalloenzyme

KW - spirochete

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